A study of the kinetics and mechanisms of metal ion transfer reactions involving peptide complexes is proposed. Copper transport in the blood involves its transfer to and from peptide coordination in serum albumin. Other metals such as nickel and cobalt may also be transported by serum albumin. Amino acid complexes are believed to play an important role in mediating the transfer of copper to low molecular weight complexes which can be readily transported across biological membranes. In the treatment of Wilson's Disease, chelating agents are used to remove copper from the body. The factors which control the pathways and rates of copper, nickel and cobalt transfer reactions will be examined. The effects of various functional groups, in combination with peptide bonding, on the properties of metal complexes will be studied, in particular the effect of sulfur-containing peptides where sulfhydryl, disulfide, or thioether groups are available for metal coordination. Factors which kinetically and thermodynamically stabilize Cu(III), Cu(II), and Cu(I) oxidation states will be examined. The major areas of investigation of metal peptide complexes include: (1) proton-transfer mechanisms, (2) metal ion transfer mechanisms to other multidentate ligands, (3) characteristics of new peptide complexes with unusual oxidation stages or metal ions not previously studied, (4) reactions of sulfur-containing ligands, (5) nature of copper transport in blood and reactions of copper in proteins where there are possible conformational changes of the proteins. A variety of stopped-flow techniques are critical to these studies and we need to extend our capabilities to include anaerobic, non-ambient systems and flow epr cells with rapid spectral scanning.